Acetyl-CoA Synthetase 2, a Mitochondrial Matrix Enzyme Involved in the Oxidation of Acetate

Takahiro Fujino, Jun Kondo, Momoyo Ishikawa, Kosuke Morikawa, Tokuo T. Yamamoto

Research output: Contribution to journalArticlepeer-review

210 Citations (Scopus)


Using peptide sequences derived from bovine cardiac acetyl-CoA synthetase (AceCS), we isolated and characterized cDNAs for a bovine and murine cardiac enzyme designated AceCS2. We also isolated a murine cDNA encoding a hepatic type enzyme, designated AceCS1, identical to one reported recently (Luong, A., Hannah, V. C., Brown, M. S., and Goldstein, J. L. (2000) J. Biol. Chem. 275, 26458-26466). Murine AceCS1 and AceCS2 were purified to homogeneity and characterized. Among C2-C5 short and medium chain fatty acids, both enzymes preferentially utilize acetate with similar affinity. The AceCS2 transcripts are expressed in a wide range of tissues, with the highest levels in heart, and are apparently absent from the liver. The levels of AceCS2 mRNA in skeletal muscle were increased markedly under ketogenic conditions. Subcellular fractionation revealed that AceCS2 is a mitochondrial matrix enzyme. [ 14C]Acetate incorporation indicated that acetyl-CoAs produced by AceCS2 are utilized mainly for oxidation.

Original languageEnglish
Pages (from-to)11420-11426
Number of pages7
JournalJournal of Biological Chemistry
Issue number14
Publication statusPublished - 2001 Apr 6

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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